The DOI matches its Crossref record; 55 of the 56 references it cites were found in a registry or an index.
Fatty liver is associated with reduced SIRT3 activity and mitochondrial protein hyperacetylation
Open accessAbstract
Acetylation has recently emerged as an important mechanism for controlling a broad array of proteins mediating cellular adaptation to metabolic fuels. Acetylation is governed, in part, by SIRTs (sirtuins), class III NAD+-dependent deacetylases that regulate lipid and glucose metabolism in liver during fasting and aging. However, the role of acetylation or SIRTs in pathogenic hepatic fuel metabolism under nutrient excess is unknown. In the present study, we isolated acetylated proteins from total liver proteome and observed 193 preferentially acetylated proteins in mice fed on an HFD (high-fat diet) compared with controls, including 11 proteins not previously identified in acetylation studies. Exposure to the HFD led to hyperacetylation of proteins involved in gluconeogenesis, mitochondrial oxidative metabolism, methionine metabolism, liver injury and the ER (endoplasmic reticulum) stress response. Livers of mice fed on the HFD had reduced SIRT3 activity, a 3-fold decrease in hepatic NAD+ levels and increased mitochondrial protein oxidation. In contrast, neither SIRT1 nor histone acetyltransferase activities were altered, implicating SIRT3 as a dominant factor contributing to the observed phenotype. In Sirt3−/− mice, exposure to the HFD further increased the acetylation status of liver proteins and reduced the activity of respiratory complexes III and IV. This is the first study to identify acetylation patterns in liver proteins of HFD-fed mice. Our results suggest that SIRT3 is an integral regulator of mitochondrial function and its depletion results in hyperacetylation of critical mitochondrial proteins that protect against hepatic lipotoxicity under conditions of nutrient excess.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Patients with NAFLD present with decreased ETC complex activity153,154 and a fatty liver-associated decrease in SIRT3 activity, which leads to hyperacetylation of mitochondrial proteins and mitochondrial dysfunction155.”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [155]
In the citing paper
“SIRT3, a member located in the mitochondria, seems to a very important role in the regulation of mitochondrial activity especially in fat metabolism”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Kendrick et al., 2011
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Increased oxidative stress in obesity and its impact on metabolic syndrome
Furukawa, S., Fujita, T., Shimabukuro, M., Iwaki, M., Yamada, Y., Nakajima, Y., Nakayama, O., Makishima, M., Matsuda, M., & Shimomura, I. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21625 · Cited by 5,508
Enzyme structure and mechanism
Fersht, A. (1977) · Medical Entomology and Zoology · Cited by 2,875
Enzyme structure and mechanism
Elmore, D. T. (1978) · Endeavour · doi:10.1016/0160-9327(78)90081-9 · Cited by 2,713
Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ
Picard, F., Kurtev, M. V., Chung, N., Topark‐Ngarm, A., Senawong, T., de Oliveira, R. M., Leid, M. E., McBurney, M. W., & Guarente, L. (2004) · Nature · doi:10.1038/nature02583 · Cited by 1,943
Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
Cohen, H. Y., Miller, C., Bitterman, K. J., Wall, N. R., Hekking, B., Kessler, B., Howitz, K. T., Gorospe, M., de Cabo, R., & Sinclair, D. A. (2004) · Science · doi:10.1126/science.1099196 · Cited by 1,924
Regulation of cellular metabolism by protein lysine acetylation
Zhao, S., Xu, W., Jiang, W., Yu, W., Lin, Y., Zhang, T., Yao, J., Zhou, L., Zeng, Y., Li, H., et al. (2010) · Science · doi:10.1126/science.1179689 · Cited by 1,910
SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., et al. (2010) · Nature · doi:10.1038/nature08778 · Cited by 1,687
Self-citationIncreased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
Tissenbaum, H. A., & Guarente, L. (2001) · Nature · doi:10.1038/35065638 · Cited by 1,603
The Sir2 Family of Protein Deacetylases
Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,497
Insulin-regulated hepatic gluconeogenesis through FOXO1–PGC-1α interaction
Puigserver, P., Rhee, J., Donovan, J., Walkey, C. J., Yoon, J. C., Oriente, F., Kitamura, Y., Altomonte, J., Dong, H., Accili, D., et al. (2003) · Nature · doi:10.1038/nature01667 · Cited by 1,487
Cited by
Sorted by citations
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
Park, J., Chen, Y., Tishkoff, D. X., Peng, C., Tan, M., Dai, L., Xie, Z., Zhang, Y., Zwaans, B. M. M., Skinner, M. E., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.001 · Cited by 1,000
Mitochondrial and metabolic dysfunction in ageing and age-related diseases
Amorim, J. A., Coppotelli, G., Rolo, A. P., Palmeira, C. M., Ross, J. M., & Sinclair, D. A. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-021-00626-7 · Cited by 990
The Role of Sirtuins in Antioxidant and Redox Signaling
Singh, C. K., Chhabra, G., Ndiaye, M. A., Garcia‐Peterson, L. M., Mack, N. J., & Ahmad, N. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7290 · Cited by 820
Sirtuin 1 and Sirtuin 3: Physiological Modulators of Metabolism
Nogueiras, R., Habegger, K. M., Chaudhary, N., Finan, B., Banks, A. S., Dietrich, M. O., Horváth, T. L., Sinclair, D. A., Pfluger, P. T., & Tschöp, M. H. (2012) · Physiological Reviews · doi:10.1152/physrev.00022.2011 · Cited by 724
Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome
Hebert, A. S., Dittenhafer-Reed, K. E., Yu, W., Bailey, D. J., Selen, E. S., Boersma, M. D., Carson, J. J., Tonelli, M., Balloon, A. J., Higbee, A. J., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.10.024 · Cited by 636
Role of Oxidative Stress in Pathophysiology of Nonalcoholic Fatty Liver Disease
Masarone, M., Rosato, V., Dallio, M., Gravina, A. G., Aglitti, A., Loguercio, C., Federico, A., & Persico, M. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9547613 · Cited by 648
Mitochondrial Sirtuin 3: New emerging biological function and therapeutic target
Zhang, J., Xiang, H., Liu, J., Chen, Y., He, R.-R., & Liu, B. (2020) · Theranostics · doi:10.7150/thno.45922 · Cited by 503
Mitochondrial Function, Biology, and Role in Disease
Murphy, E., Ardehali, H., Balaban, R. S., Lisa, F. D., Dorn, G. W., Kitsis, R. N., Otsu, K., Ping, P., Rizzuto, R., Sack, M. N., et al. (2016) · Circulation Research · doi:10.1161/res.0000000000000104 · Cited by 475
Self-citationSatapati, S., Sunny, N. E., Kucejova, B., Fu, X., He, T. T., Méndez-Lucas, A., Shelton, J. M., Perales, J. C., Browning, J. D., & Burgess, S. C. (2012) · Journal of Lipid Research · doi:10.1194/jlr.m023382 · Cited by 407
NAFLD: Mechanisms, Treatments, and Biomarkers
Nassir, F. (2022) · Biomolecules · doi:10.3390/biom12060824 · Cited by 452
Li, X. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gms108 · Cited by 360
Role of Mitochondria in Nonalcoholic Fatty Liver Disease
Nassir, F., & Ibdah, J. A. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15058713 · Cited by 369
Emerging roles of SIRT1 in fatty liver diseases
Ding, R., Bao, J., & Deng, C. (2017) · International Journal of Biological Sciences · doi:10.7150/ijbs.19370 · Cited by 364
Self-citationSIRT3-SOD2-mROS-dependent autophagy in cadmium-induced hepatotoxicity and salvage by melatonin
Pi, H., Xu, S., Reiter, R. J., Guo, P., Zhang, L., Li, Y., Li, M., Cao, Z., Tian, L., Xie, J., et al. (2015) · Autophagy · doi:10.1080/15548627.2015.1052208 · Cited by 363
Zhai, M., Li, B., Duan, W., Jing, L., Zhang, B., Zhang, M., Yu, L., Liu, Z., Yu, B., Ren, K., et al. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12419 · Cited by 354
Wang, C., Wu, S., Wu, Y., & Wei, Y. (2013) · Experimental Biology and Medicine · doi:10.1177/1535370213493069 · Cited by 321
Ansari, A., Rahman, M. S., Saha, S. K., Saikot, F. K., Deep, A., & Kim, K. (2016) · Aging Cell · doi:10.1111/acel.12538 · Cited by 315
Calorie restriction as an intervention in ageing
López‐Lluch, G., & Navas, P. (2015) · The Journal of Physiology · doi:10.1113/jp270543 · Cited by 301
Mitochondrial sirtuins: regulators of protein acylation and metabolism
He, W., Newman, J. C., Wang, M. Z., Ho, L., & Verdin, E. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.07.004 · Cited by 262
SIRT3, a pivotal actor in mitochondrial functions: metabolism, cell death and aging
Giralt, A., & Villarroya, F. (2012) · Biochemical Journal · doi:10.1042/bj20120030 · Cited by 258
Mitochondrial protein acetylation regulates metabolism
Anderson, K. A., & Hirschey, M. D. (2012) · Essays in Biochemistry · doi:10.1042/bse0520023 · Cited by 249
Non-Alcoholic Fatty Liver Disease
Engin, A. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-48382-5_19 · Cited by 253
Dual control of mitochondrial biogenesis by sirtuin 1 and sirtuin 3
Brenmoehl, J., & Hoeflich, A. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.04.002 · Cited by 248
Mitochondrial Metabolism, Sirtuins, and AgingPreprint
Sack, M. N., & Finkel, T. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013102 · Cited by 242
Self-citationThe sirtuin family’s role in aging and age-associated pathologies
Hall, J. A., Dominy, J. E., Lee, Y., & Puigserver, P. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64094 · Cited by 240
Implications of altered NAD metabolism in metabolic disorders
Okabe, K., Yaku, K., Tobe, K., & Nakagawa, T. (2019) · Journal of Biomedical Science · doi:10.1186/s12929-019-0527-8 · Cited by 223
Softic, S., Meyer, J. G., Wang, G.-X., Gupta, M. K., Batista, T. M., Lauritzen, H. P. M. M., Fujisaka, S., Serra, D., Herrero, L., Willoughby, J., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.09.003 · Cited by 227
Self-citationFrom sirtuin biology to human diseases: an update
Sebastián, C., Satterstrom, F. K., Haigis, M. C., & Mostoslavsky, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.402768 · Cited by 201
SIRT3 regulates progression and development of diseases of aging
McDonnell, E., Peterson, B. S., Bomze, H. M., & Hirschey, M. D. (2015) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2015.06.001 · Cited by 217
Alrob, O. A., Sankaralingam, S., Ma, C., Wagg, C. S., Fillmore, N., Jaswal, J. S., Sack, M. N., Lehner, R. S., Gupta, M. P., Michelakis, E. D., et al. (2014) · Cardiovascular Research · doi:10.1093/cvr/cvu156 · Cited by 223
Self-citationVariant non ketotic hyperglycinemia is caused by mutations in LIAS, BOLA3 and the novel gene GLRX5
Baker, P. R., Friederich, M. W., Swanson, M. A., Shaikh, T. H., Bhattacharya, K., Scharer, G. H., Aicher, J. K., Creadon‐Swindell, G., Geiger, E. A., Maclean, K. N., et al. (2013) · Brain · doi:10.1093/brain/awt328 · Cited by 228
Self-citationZiółkowska, S., Binienda, A., Jabłkowski, M., Szemraj, J., & Czarny, P. L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011128 · Cited by 219
Tao, R., Vassilopoulos, A., Parisiadou, L., Yan, Y., & Gius, D. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5482 · Cited by 194
Self-citationObesity II: Establishing causal links between chemical exposures and obesity
Heindel, J. J., Howard, S. G., Agay‐Shay, K., Arrebola, J. P., Audouze, K., Babin, P. J., Barouki, R., Bansal, A., Blanc, É., Cave, M. C., et al. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115015 · Cited by 220
Self-citationMammalian Sirtuins and Energy Metabolism
Li, X., & Kazgan, N. (2011) · International Journal of Biological Sciences · doi:10.7150/ijbs.7.575 · Cited by 196
Hsu, Y., Wu, Y., Yu, T.-H., & Wei, Y. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.02.011 · Cited by 189
Zheng, Y., Wang, S., Wu, J., & Wang, Y. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04367-1 · Cited by 197
SIRT3 promotes lipophagy and chaperon-mediated autophagy to protect hepatocytes against lipotoxicity
Zhang, T., Liu, J., Shen, S., Tong, Q., Ma, X., & Lin, L. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0356-z · Cited by 187
Fasting and refeeding differentially regulate NLRP3 inflammasome activation in human subjects
Traba, J., Kwarteng-Siaw, M., Okoli, T. C., Li, J., Huffstutler, R. D., Bray, A., Waclawiw, M. A., Han, K., Pelletier, M., Sauve, A. A., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci83260 · Cited by 180
Self-citationThe role of mitochondrial sirtuins in health and disease
Osborne, B., Bentley, N. L., Montgomery, M. K., & Turner, N. A. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.197 · Cited by 183
NAD+ biosynthesis, aging, and disease
Johnson, S., & Imai, S. (2018) · F1000Research · doi:10.12688/f1000research.12120.1 · Cited by 178
Zeng, X., Yang, J., Hu, O., Huang, J., Li, R., Chen, M., Zhang, Y., Zhou, X., Zhu, J., Zhang, Q., et al. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7172 · Cited by 163
The ways and means that fine tune Sirt1 activity
Revollo, J. R., & Li, X. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.12.004 · Cited by 166
Mitochondrial Roles and Cytoprotection in Chronic Liver Injury
Esposti, D. D., Hamelin, J., Bosselut, N., Saffroy, R., Sebagh, M., Pommier, A., Martel, C., & Lemoine, A. (2012) · Biochemistry Research International · doi:10.1155/2012/387626 · Cited by 165
Mitochondrial Sirtuins and Their Relationships with Metabolic Disease and Cancer
Kumar, S., & Lombard, D. B. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6213 · Cited by 161
Liu, J., Li, D., Zhang, T., Tong, Q., Ye, R. D., & Lin, L. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.564 · Cited by 161
Tao, R., Wei, D., Gao, H., Liu, Y., DePinho, R. A., & Dong, X. C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.201061 · Cited by 138
Emerging beneficial roles of sirtuins in heart failure
Tanno, M., Kuno, A., Horio, Y., & Miura, T. (2012) · Basic Research in Cardiology · doi:10.1007/s00395-012-0273-5 · Cited by 142
Wu, T., Liu, Y., Fu, Y., Liu, X., & Zhou, X.-H. (2014) · PubMed · Cited by 134
Yang, S. J., Choi, J. M., Kim, L., Park, S. E., Rhee, E., Lee, W., Oh, K. W., Park, S. W., & Park, C.-Y. (2013) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2013.09.004 · Cited by 135
Metabolic regulation by SIRT3: implications for tumorigenesis
Finley, L. W. S., & Haigis, M. C. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.05.004 · Cited by 134
Disruption of uridine homeostasis links liver pyrimidine metabolism to lipid accumulation
Le, T. T., Ziemba, A. J., Urasaki, Y., Hayes, E. D., Brotman, S. J., & Pizzorno, G. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m034249 · Cited by 131
Role of mitochondria in nonalcoholic fatty liver disease-from origin to propagation
Grattagliano, I., de Bari, O., Bernardo, T. C., Oliveira, P. J., Wang, D. Q. ‐., & Portincasa, P. (2012) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2012.03.024 · Cited by 128
Sirtuins and nonalcoholic fatty liver disease
Nassir, F., & Ibdah, J. A. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i46.10084 · Cited by 128
Nitric oxide and mitochondria in metabolic syndrome
Litvinova, L. S., Atochin, D. N., Fattakhov, N. S., Василенко, М., Затолокин, П. А., & Кириенкова, Е. В. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00020 · Cited by 132
Molecular pathways disrupted by gestational diabetes mellitus
Nguyen‐Ngo, C., Jayabalan, N., Salomón, C., & Lappas, M. (2019) · Journal of Molecular Endocrinology · doi:10.1530/jme-18-0274 · Cited by 129
Mitochondrial Sirtuins in the Regulation of Mitochondrial Activity and Metabolic Adaptation
Lombard, D. B., Tishkoff, D. X., & Bao, J. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_8 · Cited by 128
Self-citationStill, A. J., Floyd, B. J., Hebert, A. S., Bingman, C. A., Carson, J. J., Gunderson, D. R., Dolan, B. K., Grimsrud, P. A., Dittenhafer-Reed, K. E., Stapleton, D. S., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.483396 · Cited by 123
Song, B.-J., Akbar, M., Abdelmegeed, M. A., Byun, K., Lee, B., Yoon, S. K., & Hardwick, J. P. (2014) · Redox Biology · doi:10.1016/j.redox.2014.10.004 · Cited by 123
Rovira‐Llopis, S., Apostolova, N., Bañuls, C., Muntané, J., Rocha, M., & Víctor, V. M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7313 · Cited by 123
The Role of SIRT3 in Exercise and Aging
Zhou, L., Pinho, R. A., Gu, Y., & Radak, Z. O. (2022) · Cells · doi:10.3390/cells11162596 · Cited by 129
Teodoro, J. S., Duarte, F. V., Gomes, A. P., Varela, A. T. I. F., Peixoto, F., Rolo, A. P., & Palmeira, C. M. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.09.002 · Cited by 111
Biel, T. G., Lee, S., Flores‐Toro, J., Dean, J. W., Go, K. L., Lee, M.-H., Law, B. K., Law, M. E., Dunn, W. A., Zendejas, I. R., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.96 · Cited by 110
Madkour, M. I., El-Serafi, A. T., Jahrami, H., Sherif, N. M., Hassan, R. E., Awadallah, S. M., & Faris, M. E. (2019) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2019.107801 · Cited by 112
Ullah, H., Khan, A. U., Baig, M. W., Ullah, N., Ahmed, N., Tipu, M. K., Ali, H., & Khan, S. (2020) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-020-02906-7 · Cited by 109
Borengasser, S. J., Lau, F., Kang, P., Blackburn, M. L., Ronis, M. J. J., Badger, T. M., & Shankar, K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024068 · Cited by 111
Sirt3, Mitochondrial ROS, Ageing, and Carcinogenesis
Park, S., Özden, Ö., Jiang, H., Cha, Y. I., Pennington, J. D., Aykin‐Burns, N., Spitz, D. R., Gius, D. R., & Kim, H. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12096226 · Cited by 108
Self-citationProgress in Nonalcoholic Fatty Liver Disease: SIRT Family Regulates Mitochondrial Biogenesis
Zeng, C., & Chen, M. (2022) · Biomolecules · doi:10.3390/biom12081079 · Cited by 108
Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity
López-Lluch, G. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.12.005 · Cited by 103
Moschen, A. R., Wieser, V. E., Gerner, R. R., Bichler, A., Enrich, B., Moser, P. L., Ebenbichler, C. F., Kaser, S., & Tilg, H. (2013) · Journal of Hepatology · doi:10.1016/j.jhep.2013.07.027 · Cited by 103
Kwon, S., Seok, S., Yau, P. M., Li, X., KEMPER, B. W., & Kemper, J. K. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.778720 · Cited by 102
Restricted mitochondrial protein acetylation initiates mitochondrial autophagy
Webster, B. R., Scott, I., Han, K., Li, J. H., Lu, Z., Stevens, M. V., Malide, D. A., Chen, Y., Samsel, L., Connelly, P. S., et al. (2013) · Journal of Cell Science · doi:10.1242/jcs.131300 · Cited by 101
Self-citationPacella‐Ince, L., Zander‐Fox, D., & Lane, M. (2014) · Human Reproduction · doi:10.1093/humrep/deu071 · Cited by 98
The role of sirtuins in modulating redox stressors
Webster, B. R., Lu, Z., Sack, M. N., & Scott, I. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.484 · Cited by 95
Self-citationFukushima, A., & Lopaschuk, G. D. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.07.020 · Cited by 94
Targeting NAD+ in Metabolic Disease: New Insights Into an Old Molecule
Elhassan, Y., Philp, A., & Lavery, G. G. (2017) · Journal of the Endocrine Society · doi:10.1210/js.2017-00092 · Cited by 93
Role of CoA and acetyl-CoA in regulating cardiac fatty acid and glucose oxidation
Alrob, O. A., & Lopaschuk, G. D. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140094 · Cited by 95
Davies, M. N., Kjalarsdottir, L., Thompson, J. W., Dubois, L. G., Stevens, R. D., Ilkayeva, O., Brosnan, M. J., Rolph, T., Grimsrud, P. A., & Muoio, D. M. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.12.030 · Cited by 91
Lombard, D. B., & Zwaans, B. M. M. (2013) · Gerontology · doi:10.1159/000354382 · Cited by 94
Acetylation of mitochondrial proteins by GCN5L1 promotes enhanced fatty acid oxidation in the heart
Thapa, D., Zhang, M., Manning, J. R., Guimarães, D. A., Stoner, M. W., O'Doherty, R. M., Shiva, S., & Scott, I. (2017) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00752.2016 · Cited by 85
The CD38 glycohydrolase and the NAD sink: implications for pathological conditions
Zeidler, J. D., Hogan, K. A., Agorrody, G., Peclat, T., Kashyap, S., Kanamori, K. S., Gomez, L. S., Mazdeh, D. Z., Warner, G. M., Thompson, K. L., et al. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00451.2021 · Cited by 93
Sirtuins: from metabolic regulation to brain aging
Duan, W. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00036 · Cited by 89
Song, C., Fu, B., Zhang, J., Zhao, J., Yuan, M., Peng, W., Zhang, Y., & Wu, H. (2017) · Scientific Reports · doi:10.1038/s41598-017-00796-3 · Cited by 86
Berberine alleviates nonalcoholic fatty liver induced by a high‐fat diet in mice by activating SIRT3
Xu, X., Zhu, X., Bai, J., Xia, P., Li, Y., Lü, Y., Li, X.-Y., & Gao, X. (2019) · The FASEB Journal · doi:10.1096/fj.201802316r · Cited by 86
Coughlin, C. R., Scharer, G. H., Friederich, M. W., Yu, H., Geiger, E. A., Creadon‐Swindell, G., Collins, A. E., Vanlander, A. V., Coster, R. V., Powell, C. A., et al. (2015) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2015-103049 · Cited by 84
Self-citationRoles of pyruvate carboxylase in human diseases: from diabetes to cancers and infection
Lao-On, U., Attwood, P. V., & Jitrapakdee, S. (2018) · Journal of Molecular Medicine · doi:10.1007/s00109-018-1622-0 · Cited by 85
Who watches the watchmen? Regulation of the expression and activity of sirtuins
Buler, M., Andersson, U., & Hakkola, J. (2016) · The FASEB Journal · doi:10.1096/fj.201600410rr · Cited by 92
Sirtuins and the Metabolic Hurdles in Cancer
German, N. J., & Haigis, M. C. (2015) · Current Biology · doi:10.1016/j.cub.2015.05.012 · Cited by 84
Epigenetic and Disease Targets by Polyphenols
Pan, M., Lai, C., Wu, J.-C., & Ho, C. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319340010 · Cited by 86
Sirtuin 5 protects mitochondria from fragmentation and degradation during starvation
Guedouari, H., Daigle, T., Scorrano, L., & Hébert-Chatelain, É. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.10.015 · Cited by 85
Thapa, D., Wu, K., Stoner, M. W., Xie, B., Zhang, M., Manning, J. R., Lu, Z., Li, J. H., Chen, Y., Guček, M., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ac118.005462 · Cited by 85
Self-citationLi, Y., Vaitheesvaran, B., Hartil, K., Robinson, A. J., Hoopmann, M. R., Eng, J. K., Kurland, I. J., & Bruce, J. E. (2011) · Journal of Proteome Research · doi:10.1021/pr200313x · Cited by 80
Mitochondrial Dysfunction in Age‐Related Metabolic Disorders
Natarajan, V., Chawla, R., Mah, T. K. L., Vivekanandan, R., Tan, S., Sato, P. Y., & Mallilankaraman, K. B. (2020) · PROTEOMICS · doi:10.1002/pmic.201800404 · Cited by 83
Hayashi, T., Kotani, H., Yamaguchi, T., Taguchi, K., Iida, M., Ina, K., Maeda, M., Kuzuya, M., Hattori, Y., & Ignarro, L. J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1322153111 · Cited by 80
Zhu, Y., Yan, Y., Principe, D. R., Zou, X., Vassilopoulos, A., & Gius, D. R. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-15 · Cited by 77
Self-citationCardiac mitochondrial energy metabolism in heart failure: Role of cardiolipin and sirtuins
Dolinsky, V. W., Cole, L., Sparagna, G. C., & Hatch, G. M. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.03.008 · Cited by 78
Post-translational modifications of mitochondrial aldehyde dehydrogenase and biomedical implications
Song, B.-J., Abdelmegeed, M. A., Yoo, S.-H., Kim, B.-J., Jo, S. A., Jo, I., & Moon, K.-H. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.05.013 · Cited by 73
Regulation of autophagy and mitophagy by nutrient availability and acetylation
Webster, B. R., Scott, I., Traba, J., Han, K., & Sack, M. N. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.02.001 · Cited by 75
Self-citationMitochondrial Plasticity in Obesity and Diabetes Mellitus
Jeleník, T., & Roden, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4910 · Cited by 72
NAD+ repletion with niacin counteracts cancer cachexia
Beltrà, M., Pöllänen, N., Fornelli, C., Tonttila, K., Hsu, M. Y., Zampieri, S., Moletta, L., Corrà, S., Porporato, P. E., Kivelä, R., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37595-6 · Cited by 76
Metadata
- Authors
- Kendrick, A. A., Choudhury, M., Rahman, S. M., McCurdy, C. E., Friederich, M., Van Hove, J. L. K., Watson, P. A., Birdsey, N., Bao, J., Gius, D., Sack, M. N., Jing, E., Kahn, C. R., Friedman, J. E., & Jonscher, K. R.
- Affiliations
- University of Colorado Anschutz (US)
- Department of Pediatrics, University of Colorado School of Medicine, Aurora, CO 80045, U.S.A.
- Denver VA Medical Center (US)
- National Institutes of Health (US)
- Joslin Diabetes Center (US)
- ORCID
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2011-01-14
- Volume
- 433
- Issue
- 3
- Pages
- 505-514
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC3398511
- OpenAlex
- W2087439645
- Cited by
- 382
- References
- 56
- Citations by year
- 2026: 13 · 2025: 10 · 2024: 14 · 2023: 21 · 2022: 31 · 2021: 16 · 2020: 31 · 2019: 27 · 2018: 38 · 2017: 25 · 2016: 24 · 2015: 25 · 2014: 24 · 2013: 42 · 2012: 24
- FWCI
- 10.50
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical Journal (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (ZIAHL006047, ZIAHL005199)
- National Institute of Diabetes and Digestive and Kidney Diseases (R24DK085610, R01DK059767, DK59767, P30DK048520, P30-DK 48520)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (K12HD057022)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Hepatology › Liver Disease Diagnosis and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- hepatic steatosis, SIRT3, protein hyperacetylation, mitochondrial protein acetylation, high-fat diet, hepatic lipotoxicity, mitochondrial oxidative metabolism, NAD+ depletion, endoplasmic reticulum stress, gluconeogenesis, methionine metabolism, liver injury, SIRT3 knockout mice
- MeSH terms
- Acetylation, Animals, Diet, Energy Metabolism, Fatty Liver, Mice, Knockout, Cell Respiration, Mitochondrial Proteins, Proteomics, Lipid Metabolism, Mice, Sirtuin 3
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review